Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center-Reference-Cited by-同舟云学术

Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center

Published:1993-10-01 Issue:41 Volume:32 Page:11173-11180
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Thomas Jeffrey W.,Lemieux Laura J.,Alben James O.,Gennis Robert B.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00092a029

Reference40 articles.

1. Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy.

2. Infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls

3. Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex.

4. Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase

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